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. 1974 Aug;141(2):601-3.
doi: 10.1042/bj1410601.

Kinetics of irreversible enzyme inhibition by an unstable inhibitor

E T Rakitzis

Kinetics of irreversible enzyme inhibition by an unstable inhibitor

E T Rakitzis. Biochem J. 1974 Aug.

Abstract

A mathematical treatment for the general case of enzyme inactivation by an inhibitor that breaks down in solution in a first-order reaction is presented. Cathepsin D was inactivated by fluorescein isothiocyanate with a K(i) of 4.47mum. Kinetic constants were also determined for the inactivation of cathepsin D by 1,1-bis(diazoacetyl)-2-phenylethane, and the inactivation of pepsin C by diazoacetyl-dl-norleucine methyl ester.

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